The respiratory metabolism of Mycobacterium lepraemurium.

The respiratory metabolism of Mycobacterium lepraemurium isolated from Sprague-Dawley rats lepromata using several substrates was investigated. None of the intermediates of the glycolysis cycle as well as of the tricarboxylic acid cycle except succinate was oxidized by purified whole suspensions of M. lepraemurium. Likewise, many sulfur compounds such as cystine, thiourea, thioacetate, thiodiglycol, mercaptoact and some sulfhydryl compounds, e.g., cysteine, dithioerythritol, dithiorthritol, and penicillamine were readily oxidized by murine bacillary suspensions, whereas thioglycolate, thioglucose, and reduced glutathione were oxidized at a slow rate. Succinate was not or was very poorly oxidized by normal cells probably because of impermeability of the cell wall but the addition of succinate to the cell suspensions frozen for 1 min at -40 degrees C considerably enhanced oxygen uptake over the endogenous value. The oxidation of succinate was unaffected by inhibitors rotenone, atabrine, and amytal but was markedly inhibited by thenoyltrifluoroacetone, antimycin A, 2-N-heptyl-4-hydroxyquinoline-N-oxide, and cyanide. The thiol-binding agents, p-hydroxymercuribenzoate and N-ethylmaleimide were also effective inhibitors of succinate oxidation but the process was not affected by uncouplers dinitrophenol, dibromophenol, pentachlorophenol, and carbonyl-cyanide-m-chlorophenylhydrazone. The results indicated that succinate oxidation by M. lepraemurium was mediated by oxidative enzymes involving an electron transport chain with oxygen as the terminal electron acceptor.